Overview

Venoms from animals such as spiders, wasps, scorpions, and snakes contain a cocktail of bioactive proteins, peptides, and small molecules that are deadly to the intended prey. Of these, venom peptides are the most dominant component. The deleterious effect of venom peptides stem from the fact that they have evolved to target the vital receptors of their prey, resulting in paralysis, heart failure or tissue damage. These receptor targets in prey are often synonymous to some of the most sought after pharmacological human receptors, for which venom peptides exhibit a therapeutic effect. Hence, venom peptides have been touted as a rich source of new drug candidates to block pain receptors, interrupt cancer pathways, and regulate pathways in neuromuscular diseases. In addition to therapeutic drug development, venom peptides have potential in other applications such as antimicrobials, insecticides, and even siRNA delivery.

After fractionation and isolation of a venom peptide, synthetic or recombinant peptides can be useful for obtaining large amounts of the peptide for structural characterization, cellular assays, or animal studies. Known for containing multiple disulfide bonds, venom peptides can vary in length and complexity, both of which determine whether chemical or complex synthesis should be used. GenScript provides custom peptide synthesis, recombinant peptide synthesis and custom antibody production services to support your venom peptide research.

Custom peptide synthesis Recombinant peptide synthesis via
our Protein expression services

For peptides:

≤ 100 aa acids

containing 2 or less disulfide bonds

For peptides:

> 100 aa

containing more than 2 disulfide bonds

having complex secondary structure

  • Specific E. coli strain genetically engineered to facilitate the formation of disulfide bonds
  • ˃100 aa
  • Guaranteed packages for Bacterial, Mammalian, and Insect expression systems which are FREE-if-fail protected

Applications of Venom Peptides

Cone snail venom comprised of thousands of unique peptides

Cone snail venom-derived drugs are currently used for treatment of human pain and remain an attractive source for future drug discovery. For the first time, analysis of injected cone snail venom has demonstrated that the impressive diversity in venom peptides arises from a limited set of genes through a process of variable peptide processing. This processing generates conopeptides and explains how a relatively small set of gene transcripts can produce thousands of conopeptides.

Cone snail venom

Lewis et al. (2013) Deep Venomics Reveals the Mechanism for Expanded Peptide Diversity in Cone Snail Venom Molecular & Cellular Proteomics. 12, 312-329.

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This work demonstrates that selective inhibition of pain sensing voltage-gated sodium channel Nav1.7 can be achieved using peptides derived from centipede venom. This unique 46-residue peptide, µ-SLPTX-Ssm6a (Ssma6a), has high specificity for Nav1.7 and proved to be a more potent analgesic than morphine in a rodent model. This study suggests that Ssm6a might be promising in targeting Nav1.7 in human pain treatment.

Insect
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    In this study, Ssm6a was produced by recombinant expression in the periplasm of E. coli due its multiple disulfide bonds. Previously spider venom peptides were considered to be the best candidates for Nav1.7 inhibitors. However, Ssm6a was shown to have significantly higher specificity for Nav1.7 than spider venom peptides, exhibiting a more than 150-fold selectivity for Nav1.7 over other human Nav subtypes. In chemical pain tests using noxious chemical formalin, it was observed that the administration of Ssma6a was significantly more effective than morphine in reducing pain behaviors in rodent models. Ssma6a and morphine were similarly effective in reducing thermal and acid-induced pain.

Yang S et al. (2013) Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models PNAS. doi:10.1073/pnas.1306285110.

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Peptides derived from bee venom deliver siRNA to silence cancer pathways

This study demonstrates the delivery of siRNAs by peptides derived from a bee venom component called melittin. The peptides were used to deliver siRNAs that successfully decreased the production of proteins key to the NFkB pathway, which plays a central role in adult T-cell leukemia/lymphoma (ATLL), suggesting that these peptides could be useful for siRNA-targeted drug delivery.

bee
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    The siRNAs were delivered as nanoparticles, which were formed by incubation of melittin-derived peptides (known for membrane destabilization), with siRNA followed by subsequent incubation with albumin (which prevented nanoparticle flocculation). The mechanism of siRNA delivery was determined by a series of assays which revealed that the method of nanoparticle uptake was through macropinocytosis. Nanoparticle disassembly and siRNA release was activated by acidic pH, which was believed to trigger endosomal release of the siRNA cargo into the cytoplasm. When nanoparticles containing siRNAs targeting the p65 and p100/p52 protein subunits of the NFkB pathway were transfected into F8 cells, the amounts of the proteins decreased, indicating the successful silencing of protein expression in the NFkB pathway.

Tarantula venom peptide identified as an orally-active insecticide

In this study, a peptide derived from the venom of an Australian tarantula, Selenotypus plumipes was found to be an effective insecticide against termites, mealworms, and cotton bollworms. Key to the study was the ability of the peptide to be effective upon oral administration. This feat contradicts the prior belief that peptide venoms are not likely to be orally active because spider venoms are delivered through fangs and lack evolutionary pressures that would favor the robustness required for oral administration.

spider
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    In addition to insect toxicity studies, the structure of the orally active insecticidal peptide (OAIP-1), was studied by NMR spectroscopy. Custom synthesized OAIP-1 peptides were found to be a member of the knottin class of peptides, known for their internal disulfide bonds. The disulfide bond containing structure of OAIP-1, accounted for the thermal stability and protease resistance of the peptide.

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